Editors' ChoiceStructural Biology

Keeping a Kinase in Check

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Science Signaling  14 Feb 2012:
Vol. 5, Issue 211, pp. ec47
DOI: 10.1126/scisignal.2002950

Cyclic adenosine monophosphate (cAMP)–dependent protein kinase (PKA) is involved in the regulation of several key metabolic pathways. It exists in mammalian cells as an inactive tetramer composed of a regulatory (R) subunit dimer and two catalytic (C) subunits. cAMP binding causes activation by releasing the C subunits. Insight into PKA regulation has come from structures of R and C subunit heterodimers; however, further understanding requires knowledge of the holoenzyme structure. P. Zhang et al. report a high-resolution structure of the RIIβ2:C2 tetramer. The structure reveals interactions at an interface between the two RC heterodimers and provides insight into the mechanism of allosteric activation upon cAMP binding.

P. Zhang, E. V. Smith-Nguyen, M. M. Keshwani, M. S. Deal, A. P. Kornev, S. S. Taylor, Structure and allostery of the PKA RIIβ tetrameric holoenzyme. Science 335, 712–716 (2012). [Abstract] [Full Text]

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